"Helix-in-Helix" Superstructure Formation through Encapsulation of Fullerene-Bound Helical Peptides within a Helical Poly(methyl methacrylate) Cavity.

ABSTRACT: A one-handed 3₁₀ -helical hexapeptide is efficiently encapsulated within the helical cavity of st-PMMA when a fullerene (C₆₀ ) derivative is introduced at the C-terminal end of the peptide. The encapsulation is accompanied by induction of a preferred-handed helical conformation in the st-PMMA backbone with the same-handedness as that of the hexapeptide to form a crystalline st-PMMA/peptide-C₆₀ inclusion complex with a unique optically active helix-in-helix structure. Although the st-PMMA is unable to encapsulate the 3₁₀ -helical peptide without the terminal C₆₀ unit, the helical hollow space of the st-PMMA is almost filled by the C₆₀ -bound peptides. This result suggests that the C₆₀ moiety can serve as a versatil

SUBMITTER: Ousaka N 

PROVIDER: S-EPMC5248627 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature